Evidence map›Paper›PMID 26592310›Full record

ReviewCritical reviews in biochemistry and molecular biology2015

Torsins: not your typical AAA+ ATPases.

April E Rose, Rebecca S H Brown, Christian Schlieker

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.7field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. DYT-Frontiers in neuroscience · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Vesicular Acetylcholine Transporter Alters Cholinergic Tone and Synaptic Plasticity in DYT1 Dystonia.Movement disorders : official journal of the Movement Disorder Society · 2021
    Article
  16. The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.Cold Spring Harbor perspectives in biology · 2021
    Review
  17. TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

April E Rosea Department of Molecular Biophysics and Biochemistry , Yale University , New Haven , CT , USA and.
Rebecca S H Browna Department of Molecular Biophysics and Biochemistry , Yale University , New Haven , CT , USA and.
Christian Schliekera Department of Molecular Biophysics and Biochemistry , Yale University , New Haven , CT , USA and.
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Deciphering novel protein quality control pathways in the nuclear peripheryDP2OD008624 · OD · YALE UNIVERSITY · PI SCHLIEKER, CHRISTIAN DIRK · 2011 to 2011
$2.5M
NIGMS NIH HHS T32 GM007223NIH HHS DP2 OD008624NIH HHS DP2 OD008624-01
6 · The paper itself

Abstract

Torsin ATPases (Torsins) belong to the widespread AAA+ (ATPases associated with a variety of cellular activities) family of ATPases, which share structural similarity but have diverse cellular functions. Torsins are outliers in this family because they lack many characteristics of typical AAA+ proteins, and they are the only members of the AAA+ family located in the endoplasmic reticulum and contiguous perinuclear space. While it is clear that Torsins have essential roles in many, if not all metazoans, their precise cellular functions remain elusive. Studying Torsins has significant medical relevance since mutations in Torsins or Torsin-associated proteins result in a variety of congenital human disorders, the most frequent of which is early-onset torsion (DYT1) dystonia, a severe movement disorder. A better understanding of the Torsin system is needed to define the molecular etiology of these diseases, potentially enabling corrective therapy. Here, we provide a comprehensive overview of the Torsin system in metazoans, discuss functional clues obtained from various model systems and organisms and provide a phylogenetic and structural analysis of Torsins and their regulatory cofactors in relation to disease-causative mutations. Moreover, we review recent data that have led to a dramatically improved understanding of these machines at a molecular level, providing a foundation for investigating the molecular defects underlying the associated movement disorders. Lastly, we discuss our ideas on how recent progress may be utilized to inform future studies aimed at determining the cellular role(s) of these atypical molecular machines and their implications for dystonia treatment options.

Indexed as

Amino Acid SequenceAnimalsCarrier ProteinsDisease Models, AnimalDystonia Musculorum DeformansHSC70 Heat-Shock ProteinsHumansMembrane ProteinsMolecular ChaperonesMolecular Sequence DataMutationProtein TransportSequence AlignmentCarrier ProteinsHSC70 Heat-Shock ProteinsHSPA8 protein, humanMembrane ProteinsMolecular ChaperonesTOR1AIP2 protein, humanTOR1A protein, humanEarly-onset torsion dystoniaendoplasmic reticulumLAP1LULL1nuclear envelopetorsinA

Identifiers

PMID26592310
PMCPMC4872298
OpenAlexW1805914897

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.